BAG3 Gene

Name	BCL2-associated athanogene 3
Description	BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The protein encoded by this gene contains a WW domain in the N-terminal region and a BAG domain in the C-terminal region. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner. [provided by RefSeq, Jul 2008]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n BAG3 (Bcl‐2–associated athanogene 3) is a multifunctional, stress‐inducible co‐chaperone that interacts with Hsp70 via its canonical BAG domain and with small heat shock proteins (sHsps) through conserved IPV motifs. In this capacity, BAG3 plays a central role in protein quality control by coordinating the recognition and autophagic clearance of misfolded and aggregation‐prone proteins—such as mutant huntingtin, mutant SOD1, and others—by facilitating their transport to aggresomes and subsequent degradation (see."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "5"}]}, {"type": "t", "text": " Moreover, by altering the balance between proteasomal and autophagic degradation pathways—particularly under conditions of proteasome impairment—BAG3 helps reroute ubiquitinated clients to autophagosomes (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n In addition to its functions in proteostasis, BAG3 is critically involved in maintaining cytoskeletal integrity and cell architecture. Its localization to the sarcomeric Z‐disk in striated muscle and its ability to stabilize actin‐capping proteins (e.g., CapZβ1) ensure proper myofibril organization and resistance to mechanical stress (see."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "9"}]}, {"type": "t", "text": " Disruption of BAG3 function—whether by mutation or altered expression—compromises these processes and is implicated in the pathogenesis of muscle degeneration, including dilated cardiomyopathy and severe myofibrillar myopathies (see."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "14"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n BAG3 also modulates oncogenic signaling. By interacting with partners such as Hsp70 and the Src SH3 domain, it influences pathways that promote cell survival, migration, and metastasis. High BAG3 expression in several tumor types supports cancer cell growth by activating NF‐κB signaling and inhibiting apoptosis; indeed, pharmacological disruption of the Hsp70–BAG3 complex impairs these signals and suppresses tumor progression (see."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "20"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Finally, BAG3 expression is subject to regulation by epigenetic mechanisms, including microRNAs, which further underscores its role in diverse cellular contexts ranging from stress adaptation and cytoskeletal maintenance to cardiac function and tumor progression (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "21"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Overall, BAG3 functions as a central hub integrating stress response, chaperone‐mediated protein quality control, cytoskeletal organization, and signal transduction to ensure cellular homeostasis and adaptability under conditions of stress.\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Serena Carra, Samuel J Seguin, Herman Lambert, et al. "}, {"type": "b", "children": [{"type": "t", "text": "HspB8 chaperone activity toward poly(Q)-containing proteins depends on its association with Bag3, a stimulator of macroautophagy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M706304200"}], "href": "https://doi.org/10.1074/jbc.M706304200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18006506"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18006506"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Martin Gamerdinger, A Murat Kaya, Uwe Wolfrum, et al. "}, {"type": "b", "children": [{"type": "t", "text": "BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO Rep (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/embor.2010.203"}], "href": "https://doi.org/10.1038/embor.2010.203"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21252941"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21252941"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Valeria Crippa, Daniela Sau, Paola Rusmini, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The small heat shock protein B8 (HspB8) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Mol Genet (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/hmg/ddq257"}], "href": "https://doi.org/10.1093/hmg/ddq257"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20570967"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20570967"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Serena Carra, Samuel J Seguin, Jacques Landry "}, {"type": "b", "children": [{"type": "t", "text": "HspB8 and Bag3: a new chaperone complex targeting misfolded proteins to macroautophagy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Autophagy (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4161/auto.5407"}], "href": "https://doi.org/10.4161/auto.5407"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18094623"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18094623"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Jennifer N Rauch, Eric Tse, Rebecca Freilich, et al. "}, {"type": "b", "children": [{"type": "t", "text": "BAG3 Is a Modular, Scaffolding Protein that physically Links Heat Shock Protein 70 (Hsp70) to the Small Heat Shock Proteins."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Mol Biol (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.jmb.2016.11.013"}], "href": "https://doi.org/10.1016/j.jmb.2016.11.013"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27884606"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27884606"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Melania Minoia, Alessandra Boncoraglio, Jonathan Vinet, et al. "}, {"type": "b", "children": [{"type": "t", "text": "BAG3 induces the sequestration of proteasomal clients into cytoplasmic puncta: implications for a proteasome-to-autophagy switch."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Autophagy (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4161/auto.29409"}], "href": "https://doi.org/10.4161/auto.29409"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25046115"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25046115"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "A Rosati, V Graziano, V De Laurenzi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "BAG3: a multifaceted protein that regulates major cell pathways."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Death Dis (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/cddis.2011.24"}], "href": "https://doi.org/10.1038/cddis.2011.24"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21472004"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21472004"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Sachiko Homma, Masahiro Iwasaki, G Diane Shelton, et al. "}, {"type": "b", "children": [{"type": "t", "text": "BAG3 deficiency results in fulminant myopathy and early lethality."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Pathol (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.2353/ajpath.2006.060250"}], "href": "https://doi.org/10.2353/ajpath.2006.060250"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16936253"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16936253"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Akinori Hishiya, Toshio Kitazawa, Shinichi Takayama "}, {"type": "b", "children": [{"type": "t", "text": "BAG3 and Hsc70 interact with actin capping protein CapZ to maintain myofibrillar integrity under mechanical stress."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Circ Res (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1161/CIRCRESAHA.110.225649"}], "href": "https://doi.org/10.1161/CIRCRESAHA.110.225649"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20884878"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20884878"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Duygu Selcen, Francesco Muntoni, Barbara K Burton, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mutation in BAG3 causes severe dominant childhood muscular dystrophy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Ann Neurol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/ana.21553"}], "href": "https://doi.org/10.1002/ana.21553"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19085932"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19085932"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Nadine Norton, Duanxiang Li, Mark J Rieder, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Genome-wide studies of copy number variation and exome sequencing identify rare variants in BAG3 as a cause of dilated cardiomyopathy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Hum Genet (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.ajhg.2011.01.016"}], "href": "https://doi.org/10.1016/j.ajhg.2011.01.016"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21353195"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21353195"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Karin Y van Spaendonck-Zwarts, Anna Posafalvi, Maarten P van den Berg, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Titin gene mutations are common in families with both peripartum cardiomyopathy and dilated cardiomyopathy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Eur Heart J (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/eurheartj/ehu050"}], "href": "https://doi.org/10.1093/eurheartj/ehu050"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24558114"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24558114"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Xi Fang, Julius Bogomolovas, Tongbin Wu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Loss-of-function mutations in co-chaperone BAG3 destabilize small HSPs and cause cardiomyopathy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Clin Invest (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1172/JCI94310"}], "href": "https://doi.org/10.1172/JCI94310"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28737513"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28737513"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Fernando Domínguez, Sofía Cuenca, Zofia Bilińska, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Dilated Cardiomyopathy Due to BLC2-Associated Athanogene 3 (BAG3) Mutations."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Am Coll Cardiol (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.jacc.2018.08.2181"}], "href": "https://doi.org/10.1016/j.jacc.2018.08.2181"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30442290"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30442290"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "M Y Sherman, V L Gabai "}, {"type": "b", "children": [{"type": "t", "text": "Hsp70 in cancer: back to the future."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/onc.2014.349"}], "href": "https://doi.org/10.1038/onc.2014.349"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25347739"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25347739"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Teresa A Colvin, Vladimir L Gabai, Jianlin Gong, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Hsp70-Bag3 interactions regulate cancer-related signaling networks."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Res (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/0008-5472.CAN-14-0747"}], "href": "https://doi.org/10.1158/0008-5472.CAN-14-0747"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24994713"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24994713"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Massimo Ammirante, Alessandra Rosati, Claudio Arra, et al. "}, {"type": "b", "children": [{"type": "t", "text": "IKK{gamma} protein is a target of BAG3 regulatory activity in human tumor growth."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0907696107"}], "href": "https://doi.org/10.1073/pnas.0907696107"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20368414"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20368414"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Michelina Festa, Luis Del Valle, Kamel Khalili, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "MicroRNA 345, a methylation-sensitive microRNA is involved in cell proliferation and invasion in human colorectal cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Carcinogenesis (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/carcin/bgr114"}], "href": "https://doi.org/10.1093/carcin/bgr114"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21665895"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21665895"}]}]}]}
Synonyms	BAG-3, MFM6, CAIR-1, BIS
Proteins	BAG3_HUMAN
NCBI Gene ID	9531
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

BAG3 has 12,961 functional associations with biological entities spanning 9 categories (molecular profile, organism, disease, phenotype or trait, chemical, functional term, phrase or reference, structural feature, cell line, cell type or tissue, gene, protein or microRNA, sequence feature) extracted from 133 datasets.

Click the + buttons to view associations for BAG3 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

BAG3 Gene

Functional Associations

Please acknowledge the Harmonizome in your publications by citing the following reference(s):

	Dataset	Summary
	Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of BAG3 gene relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray	tissue samples with high or low expression of BAG3 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq	tissue samples with high or low expression of BAG3 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq dataset.
	Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of BAG3 gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
	BioGPS Cell Line Gene Expression Profiles	cell lines with high or low expression of BAG3 gene relative to other cell lines from the BioGPS Cell Line Gene Expression Profiles dataset.
	BioGPS Human Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of BAG3 gene relative to other cell types and tissues from the BioGPS Human Cell Type and Tissue Gene Expression Profiles dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of BAG3 gene relative to other cell lines from the CCLE Cell Line Gene CNV Profiles dataset.
	CCLE Cell Line Gene Expression Profiles	cell lines with high or low expression of BAG3 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with BAG3 protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with BAG3 gene from the CellMarker Gene-Cell Type Associations dataset.
	ChEA Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of BAG3 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of BAG3 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets dataset.
	ChEA Transcription Factor Targets 2022	transcription factors binding the promoter of BAG3 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	ClinVar Gene-Phenotype Associations	phenotypes associated with BAG3 gene from the curated ClinVar Gene-Phenotype Associations dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of BAG3 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing BAG3 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing BAG3 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores	cellular components containing BAG3 protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores 2025	cellular components containing BAG3 protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with BAG3 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025	cellular components co-occuring with BAG3 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	COSMIC Cell Line Gene CNV Profiles	cell lines with high or low copy number of BAG3 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with BAG3 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with BAG3 gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with BAG3 gene/protein from the curated CTD Gene-Disease Associations dataset.
	dbGAP Gene-Trait Associations	traits associated with BAG3 gene in GWAS and other genetic association datasets from the dbGAP Gene-Trait Associations dataset.
	DeepCoverMOA Drug Mechanisms of Action	small molecule perturbations with high or low expression of BAG3 protein relative to other small molecule perturbations from the DeepCoverMOA Drug Mechanisms of Action dataset.
	DepMap CRISPR Gene Dependency	cell lines with fitness changed by BAG3 gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DISEASES Curated Gene-Disease Association Evidence Scores	diseases involving BAG3 gene from the DISEASES Curated Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Curated Gene-Disease Association Evidence Scores 2025	diseases involving BAG3 gene from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores	diseases associated with BAG3 gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores 2025	diseases associated with BAG3 gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores 2025 dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with BAG3 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores 2025	diseases co-occuring with BAG3 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.
	DisGeNET Gene-Disease Associations	diseases associated with BAG3 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with BAG3 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Phenoptype Associations dataset.
	ENCODE Histone Modification Site Profiles	histone modification site profiles with high histone modification abundance at BAG3 gene from the ENCODE Histone Modification Site Profiles dataset.
	ENCODE Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of BAG3 gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of BAG3 gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset.
	ESCAPE Omics Signatures of Genes and Proteins for Stem Cells	PubMedIDs of publications reporting gene signatures containing BAG3 from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.